This study has as its objectives the elucidation of the physical properties of the alpha crystallin of the lens. Studies will be undertaken of the dissociation reactions of alpha crystallin (ca 7 X 10 to the fifth power daltons) in various solutions particularly the alkaline region, pH 10-118. This could help to understand the assembly of alpha crystallin from the polypeptide level (gene product and modified gene product). Alpha crystallin of the lens give rise to aggregated units which vary with regard to the region of the lens. The factors involved will be explored, particularly the effect of temperature, Ca ion concentration, and various sugars and polyhydric alcohols. The methods used for these studies will be velocity and equilibrium sedimentation, viscosity, light scattering, electrophoretic techniques, and column chromatography on both ion exchange and molecular siene materials. The sources for the alpha crystallin will be ovine, porcine, and bovine lens.